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Q5J6J3

- DPP4_TRIRU

UniProt

Q5J6J3 - DPP4_TRIRU

Protein

Dipeptidyl peptidase 4

Gene

DPP4

Organism
Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 38 (01 Oct 2014)
      Sequence version 1 (15 Feb 2005)
      Previous versions | rss
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    Functioni

    Extracellular dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Contributes to pathogenicity.1 Publication

    Catalytic activityi

    Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.PROSITE-ProRule annotation

    pH dependencei

    Optimum pH is 7.0-9.0.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei613 – 6131Charge relay systemPROSITE-ProRule annotation
    Active sitei690 – 6901Charge relay systemPROSITE-ProRule annotation
    Active sitei725 – 7251Charge relay systemPROSITE-ProRule annotation

    GO - Molecular functioni

    1. aminopeptidase activity Source: UniProtKB-KW
    2. serine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. pathogenesis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Virulence

    Protein family/group databases

    MEROPSiS09.008.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dipeptidyl peptidase 4 (EC:3.4.14.5)
    Alternative name(s):
    Dipeptidyl peptidase IV
    Short name:
    DPP IV
    Short name:
    DppIV
    Gene namesi
    Name:DPP4
    OrganismiTrichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum)
    Taxonomic identifieri5551 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaemitosporic ArthrodermataceaeTrichophyton

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. membrane Source: InterPro

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1515Sequence AnalysisAdd
    BLAST
    Chaini16 – 775760Dipeptidyl peptidase 4PRO_0000384089Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi219 – 2191N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ5J6J3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S9B family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.140.10.30. 1 hit.
    3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR002471. Pept_S9_AS.
    IPR001375. Peptidase_S9.
    IPR002469. Peptidase_S9B.
    [Graphical view]
    PfamiPF00930. DPPIV_N. 1 hit.
    PF00326. Peptidase_S9. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00131. CARBOXYPEPT_SER_SER. 1 hit.
    PS00708. PRO_ENDOPEP_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q5J6J3-1 [UniParc]FASTAAdd to Basket

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    MKLLSLLMLA GIAQAIVPPR EPRSPTGGGN KLLTYKECVP RATISPRSTS    50
    LAWINSEEDG RYISQSDDGA LILQNIVTNT NKTLVAADKV PKGYYDYWFK 100
    PDLSAVLWAT NYTKQYRHSY FANYFILDIK KGSLTPLAQD QAGDIQYAQW 150
    SPMNNSIAYV RXNDLYIWNN GKTKRITENG GPDIFNGVPD WVYEEEIFGD 200
    RFALWFSPDG EYLAYLRFNE TGVPTYTIPY YKNKQKIAPA YPRELEIRYP 250
    KVSAKNPTVQ FHLLNIASSQ ETTIPVTAFP ENDLVIGEVA WLSSGHDSVA 300
    YRAFNRVQDR EKIVSVKVES KESKVIRERD GTDGWIDNLL SMSYIGNVNG 350
    KEYYVDISDA SGWAHIYLYP VDGGKEIALT KGEWEVVAIL KVDTKKKLIY 400
    FTSTKYHSTT RHVYSVSYDT KVMTPLVNDK EAAYYTASFS AKGGYYILSY 450
    QGPNVPYQEL YSTKDSKKPL KTITSNDALL EKLKEYKLPK VSFFEIKLPS 500
    GETLNVKQRL PPNFNPHKKY PVLFTPYGGP GAQEVSQAWN SLDFKSYITS 550
    DPELEYVTWT VDNRGTGYKG RKFRSAVAKR LGFLEAQDQV FAAKEVLKNR 600
    WADKDHIGIW GXSYGGFLTA KTLETDSGVF TFGISTAPVS DFRLYDSMYT 650
    ERYMKTVELN ADGYSETAVH KVDGFKNLKG HYLIQHGTGD DNVHFQNAAV 700
    LSNTLMNGGV TADKLTTQWF TDSDHGIRYD MDSTYQYKQL SKMVYDQKQR 750
    RPESPPMHQW SKRVLAALFG ERAEE 775
    Length:775
    Mass (Da):88,021
    Last modified:February 15, 2005 - v1
    Checksum:i157774F128C6BFDB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY497021 Genomic DNA. Translation: AAS76665.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY497021 Genomic DNA. Translation: AAS76665.1 .

    3D structure databases

    ProteinModelPortali Q5J6J3.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S09.008.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.140.10.30. 1 hit.
    3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR002471. Pept_S9_AS.
    IPR001375. Peptidase_S9.
    IPR002469. Peptidase_S9B.
    [Graphical view ]
    Pfami PF00930. DPPIV_N. 1 hit.
    PF00326. Peptidase_S9. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00131. CARBOXYPEPT_SER_SER. 1 hit.
    PS00708. PRO_ENDOPEP_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Aminopeptidases and dipeptidyl-peptidases secreted by the dermatophyte Trichophyton rubrum."
      Monod M., Lechenne B., Jousson O., Grand D., Zaugg C., Stoecklin R., Grouzmann E.
      Microbiology 151:145-155(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiDPP4_TRIRU
    AccessioniPrimary (citable) accession number: Q5J6J3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 38 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3